Publication

The fourth helical secondary structure of β-peptides: The (P)-28-helix of a β-hexapeptide consisting of (2R,3S)-3-amino-2-hydroxy acid residues

Karl Gademann
2003
Journal paper

Abstract

The authors report compelling evidence for the formation of a fourth type of helical secondary structure of a beta-peptide in MeOH, and this phenomenon occurs if each amino acid has a hydroxy group in the 2-position. 2D-NMR expts. of terminally-protected beta-hexapeptide I were conducted to obtain its secondary structure information.

Official source

https://infoscience.epfl.ch/record/95748?ln=en

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The fourth helical secondary structure of β-peptides: The (P)-28-helix of a β-hexapeptide consisting of (2R,3S)-3-amino-2-hydroxy acid residues

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